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Title: Preliminary X-Ray Crystallographic Studies of the N-Terminal Domains of Hsp104 from Yeast Candida albicans and Saccharomyces cerevisiae

Journal Article · · Crystallography Reports
;  [1]
  1. University of Alabama at Birmingham, Department of Cell, Developmental and Integrative Biology (CDIB) (United States)

Yeast Hsp104 is an ATP-dependent molecular chaperone, which can solublize and rescue denatured proteins from aggregates into active form by cooperating with Hsp70 and Hsp40 chaperones. Moreover, overexpression of Hsp104 of Saccharomyces cerevisiae (ScHsp104) cures the yeast [PSI{sup +}] prion due to the completely dissolution of the prion seeds, demonstrating ScHsp104’s potential to clear amyloid-like protein aggregates, thus making ScHsp104 a promising medication approach for human amyloidogenic neurodegenerative diseases. Because the working mechanisms for ScHsp104’s activities have not been clearly elucidated yet, crystallographic determination of ScHsp104 stands for great significance. Here, the expression, purification and crystallization of the N-terminal domains of Hsp104 from yeast Candida albicans (CaHsp104N) and S. cerevisiae (ScHsp104N) are described. The CaHsp104N crystals diffracted to 1.54 Å and belonged to the sp. gr. P3{sub 2}21 or P3{sub 1}21, with unit cell parameters of a = 55.213 Å, c = 109.451 Å. The data of the ScHsp104N crystals were collected to the resolution of 2.53 Å in the sp. gr. C2, with unit cell parameters a = 148.587 Å, b = 66.255 Å, c = 74.577 Å, β = 107.369°. The phase of ScHsp104N is determined by the molecular replacement method using CaHsp104N as the search model.

OSTI ID:
22758286
Journal Information:
Crystallography Reports, Vol. 62, Issue 7; Other Information: Copyright (c) 2017 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
Country of Publication:
United States
Language:
English